Capn2 (calpain 2) - Rat Genome Database

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Gene: Capn2 (calpain 2) Rattus norvegicus
Analyze
Symbol: Capn2
Name: calpain 2
RGD ID: 2268
Description: Enables calcium ion binding activity; cytoskeletal protein binding activity; and enzyme binding activity. Contributes to calcium-dependent cysteine-type endopeptidase activity. Involved in several processes, including cellular response to interferon-beta; positive regulation of cardiac muscle cell apoptotic process; and positive regulation of myoblast fusion. Located in several cellular components, including external side of plasma membrane; focal adhesion; and neuronal cell body. Biomarker of hypertrophic cardiomyopathy; sciatic neuropathy; and traumatic brain injury. Orthologous to human CAPN2 (calpain 2); PARTICIPATES IN the proteolytic pathway involving calcium-dependent proteases; Alzheimer's disease pathway; apoptotic cell death pathway; INTERACTS WITH 2,3,7,8-tetrachlorodibenzodioxine; 2,4-dinitrotoluene; 2,6-dinitrotoluene.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: calcium-activated neutral proteinase 2; calpain 2, (m/II) large subunit; calpain II; calpain M-type; calpain-2 catalytic subunit; calpain-2 large subunit; CANP 2; M-calpain; millimolar-calpain
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Alliance Orthologs
More Info more info ...
Latest Assembly: GRCr8 - GRCr8 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81396,681,902 - 96,732,625 (-)NCBIGRCr8
mRatBN7.21394,150,244 - 94,200,969 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1394,150,240 - 94,200,969 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1396,655,495 - 96,706,202 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01398,055,407 - 98,106,133 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01395,237,587 - 95,288,310 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.013100,878,649 - 100,928,811 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl13100,878,650 - 100,928,811 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.013105,814,749 - 105,864,911 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41398,473,367 - 98,524,463 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.11398,662,303 - 98,713,399 (-)NCBI
Celera1393,683,410 - 93,734,060 (-)NCBICelera
Cytogenetic Map13q26NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(-)-epigallocatechin 3-gallate  (ISO)
1,2-dimethylhydrazine  (ISO)
17beta-estradiol  (ISO)
17beta-hydroxy-5alpha-androstan-3-one  (ISO)
2,2',4,4'-Tetrabromodiphenyl ether  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4,6-tribromophenol  (ISO)
2,4-dinitrotoluene  (EXP)
2,6-di-tert-butyl-4-methylphenol  (ISO)
2,6-dimethoxyphenol  (ISO)
2,6-dinitrotoluene  (EXP)
3,3',5,5'-tetrabromobisphenol A  (ISO)
3-chloropropane-1,2-diol  (EXP)
3-isobutyl-1-methyl-7H-xanthine  (ISO)
3H-1,2-dithiole-3-thione  (EXP)
4,4'-sulfonyldiphenol  (ISO)
4-[1-hydroxy-2-[4-(phenylmethyl)-1-piperidinyl]propyl]phenol  (EXP)
4-\{[(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)carbonyl]amino\}benzoic acid  (ISO)
4-aminophenol  (EXP)
4-hydroxynon-2-enal  (ISO)
4-phenylbutyric acid  (ISO)
5-aza-2'-deoxycytidine  (ISO)
6alpha-methylprednisolone  (EXP)
8-Br-cAMP  (ISO)
9-cis-retinoic acid  (ISO)
acetamide  (EXP)
acetylleucyl-leucyl-norleucinal  (ISO)
acetylsalicylic acid  (ISO)
acrolein  (ISO)
acrylamide  (EXP,ISO)
actinomycin D  (ISO)
aflatoxin B1  (ISO)
agomelatine  (EXP)
all-trans-retinoic acid  (ISO)
Ammothamnine  (ISO)
anthra[1,9-cd]pyrazol-6(2H)-one  (EXP)
aristolochic acid A  (ISO)
Aroclor 1254  (ISO)
arsenite(3-)  (ISO)
arsenous acid  (ISO)
atrazine  (EXP)
BAPTA  (ISO)
benzo[a]pyrene  (ISO)
benzo[e]pyrene  (ISO)
beta-lapachone  (ISO)
bis(2-ethylhexyl) phthalate  (ISO)
bisphenol A  (EXP,ISO)
bisphenol AF  (ISO)
Bisphenol B  (ISO)
bisphenol F  (ISO)
bucladesine  (ISO)
cadmium atom  (ISO)
cadmium dichloride  (ISO)
caffeine  (ISO)
calcitriol  (ISO)
Calpeptin  (EXP)
cannabidiol  (ISO)
cantharidin  (ISO)
carbamazepine  (ISO)
carbon disulfide  (EXP)
carbon nanotube  (ISO)
casticin  (ISO)
chlordecone  (ISO)
chloroacetic acid  (ISO)
cisplatin  (EXP,ISO)
clofibrate  (ISO)
cobalt dichloride  (ISO)
copper(II) sulfate  (ISO)
crocidolite asbestos  (ISO)
Cuprizon  (ISO)
cyclophosphamide  (ISO)
cyclosporin A  (ISO)
dantrolene  (EXP)
DDT  (EXP)
dexamethasone  (EXP,ISO)
diarsenic trioxide  (ISO)
dibenzo[a,l]pyrene  (ISO)
dicrotophos  (ISO)
diethylstilbestrol  (ISO)
diuron  (EXP)
dorsomorphin  (ISO)
endosulfan  (EXP)
epoxiconazole  (ISO)
ethanol  (EXP,ISO)
ethylene glycol bis(2-aminoethyl)tetraacetic acid  (ISO)
fipronil  (EXP)
fisetin  (ISO)
folic acid  (ISO)
fumonisin B1  (ISO)
furfural  (ISO)
geneticin  (ISO)
gentamycin  (EXP)
glimepiride  (ISO)
glyburide  (ISO)
heparin  (ISO)
Honokiol  (ISO)
hydrogen peroxide  (EXP,ISO)
hydroquinone  (ISO)
indometacin  (EXP,ISO)
isoflurane  (EXP)
isoprenaline  (EXP)
ivermectin  (ISO)
lipopolysaccharide  (ISO)
medroxyprogesterone acetate  (ISO)
menadione  (ISO)
methapyrilene  (ISO)
methimazole  (EXP)
methoxychlor  (EXP)
methylmercury chloride  (ISO)
microcystin-LR  (ISO)
N-acetyl-L-cysteine  (ISO)
N-methyl-D-aspartic acid  (EXP)
N-methyl-N-nitrosourea  (EXP)
N-nitrosodimethylamine  (ISO)
nickel atom  (ISO)
nimesulide  (EXP)
nitrates  (ISO)
nitroglycerin  (EXP)
NS-398  (EXP)
Nutlin-3  (ISO)
ozone  (ISO)
paracetamol  (EXP,ISO)
paraoxon  (ISO)
paraquat  (EXP)
phenethyl isothiocyanate  (EXP)
phenobarbital  (ISO)
phenylmercury acetate  (ISO)
pirinixic acid  (ISO)
pregnenolone 16alpha-carbonitrile  (EXP)
procaine  (ISO)
propiconazole  (ISO)
quercetin  (EXP,ISO)
raloxifene  (ISO)
SB 431542  (ISO)
sodium arsenite  (EXP,ISO)
sodium chloride  (ISO)
surfactin  (ISO)
surfactin C  (ISO)
tamoxifen  (ISO)
temozolomide  (ISO)
tert-butyl hydroperoxide  (ISO)
testosterone  (EXP,ISO)
testosterone enanthate  (ISO)
tetrachloromethane  (EXP,ISO)
thioacetamide  (EXP)
titanium dioxide  (ISO)
trichostatin A  (EXP)
triphenyl phosphate  (ISO)
Triptolide  (ISO)
tungsten  (ISO)
ursodeoxycholic acid  (EXP)
valproic acid  (ISO)
vancomycin  (ISO)
vildagliptin  (EXP)
vorinostat  (ISO)
Z-Val-Phe-H  (EXP)

Gene Ontology Annotations     Click to see Annotation Detail View

Cellular Component

Molecular Function

References

References - curated
# Reference Title Reference Citation
1. Contribution of distinct structural elements to activation of calpain by Ca2+ ions. Alexa A, etal., J Biol Chem. 2004 May 7;279(19):20118-26. Epub 2004 Feb 19.
2. An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits myoblast fusion. Balcerzak D, etal., J Cell Sci. 1995 May;108 ( Pt 5):2077-82.
3. Knockdown of m-calpain increases survival of primary hippocampal neurons following NMDA excitotoxicity. Bevers MB, etal., J Neurochem. 2009 Mar;108(5):1237-50. doi: 10.1111/j.1471-4159.2008.05860.x. Epub 2009 Jan 22.
4. Proteomic study of calpain interacting proteins during skeletal muscle aging. Brulé C, etal., Biochimie. 2010 Dec;92(12):1923-33. doi: 10.1016/j.biochi.2010.09.003. Epub 2010 Sep 17.
5. Nuclear translocation of calpain-2 regulates propensity toward apoptosis in cardiomyocytes of tail-suspended rats. Chang H, etal., J Cell Biochem. 2011 Feb;112(2):571-80. doi: 10.1002/jcb.22947.
6. Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit. DeLuca CI, etal., Biochim Biophys Acta 1993 Oct 19;1216(1):81-93.
7. Myoblast fusion requires fibronectin degradation by exteriorized m-calpain. Dourdin N, etal., Exp Cell Res. 1997 Sep 15;235(2):385-94. doi: 10.1006/excr.1997.3684.
8. Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle. Enns DL, etal., Eur J Appl Physiol. 2007 Jul;100(4):445-55. Epub 2007 Apr 12.
9. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
10. Active recombinant rat calpain II. Bacterially produced large and small subunits associate both in vivo and in vitro. Graham-Siegenthaler K, etal., J Biol Chem 1994 Dec 2;269(48):30457-60.
11. Calpastatin simultaneously binds four calpains with different kinetic constants. Hanna RA, etal., FEBS Lett. 2007 Jun 26;581(16):2894-8. Epub 2007 May 25.
12. Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. Hanna RA, etal., Nature. 2008 Nov 20;456(7220):409-12. doi: 10.1038/nature07451.
13. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. Hosfield CM, etal., EMBO J. 1999 Dec 15;18(24):6880-9.
14. Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides. Hosfield CM, etal., J Mol Biol. 2004 Oct 29;343(4):1049-53.
15. Calpain 2 activity increases at the time of implantation in rat uterine luminal epithelial cells and administration of calpain inhibitor significantly reduces implantation sites. Kaneko Y, etal., Histochem Cell Biol. 2014 Apr;141(4):423-30. doi: 10.1007/s00418-013-1165-y. Epub 2013 Nov 23.
16. Inhibition of myelin-cleaving poteolytic activities by interferon-beta in rat astrocyte cultures. Comparative analysis between gelatinases and calpain-II. Latronico T, etal., PLoS One. 2013;8(2):e49656. doi: 10.1371/journal.pone.0049656. Epub 2013 Feb 4.
17. An antisense oligodeoxyribonucleotide to m-calpain mRNA inhibits secretion from alveolar epithelial type II cells. Li HL, etal., Cell Signal. 1998 Feb;10(2):137-42.
18. An intracellular serpin regulates necrosis by inhibiting the induction and sequelae of lysosomal injury. Luke CJ, etal., Cell. 2007 Sep 21;130(6):1108-19.
19. Influence of electrical stimulation on calpain and ubiquitin-proteasome systems in the denervated and unloaded rat tibialis anterior muscles. Matsumoto A, etal., Acta Histochem. 2014 Jun;116(5):936-42. doi: 10.1016/j.acthis.2014.03.006. Epub 2014 Apr 16.
20. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
21. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Moldoveanu T, etal., Nature. 2008 Nov 20;456(7220):404-8.
22. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
23. Mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria. Ozaki T, etal., Biochim Biophys Acta. 2009 Dec;1793(12):1848-59. doi: 10.1016/j.bbamcr.2009.10.002. Epub 2009 Oct 13.
24. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
25. Calpain and calpastatin expression in primary oligodendrocyte culture: preferential localization of membrane calpain in cell processes. Ray SK, etal., J Neurosci Res. 2002 Nov 15;70(4):561-9. doi: 10.1002/jnr.10414.
26. GOA pipeline RGD automated data pipeline
27. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
28. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
29. Effects of injury severity on regional and temporal mRNA expression levels of calpains and caspases after traumatic brain injury in rats. Ringger NC, etal., J Neurotrauma. 2004 Jul;21(7):829-41.
30. Nuclear Translocation of Calpain-2 Mediates Apoptosis of Hypertrophied Cardiomyocytes in Transverse Aortic Constriction Rat. Sheng JJ, etal., J Cell Physiol. 2015 Nov;230(11):2743-54. doi: 10.1002/jcp.24999.
31. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
32. Proteolysis of neuronal cytoskeletal proteins by calpain contributes to rat retinal cell death induced by hypoxia. Tamada Y, etal., Brain Res. 2005 Jul 19;1050(1-2):148-55.
33. m-Calpain (calcium-activated neutral proteinase) in Alzheimer's disease brains. Tsuji T, etal., Neurosci Lett. 1998 May 29;248(2):109-12.
34. Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy. Vermaelen M, etal., Am J Physiol Cell Physiol. 2007 May;292(5):C1723-31. Epub 2006 Dec 20.
35. Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neurons. Wang CF and Huang YS, Mol Cell Biol. 2012 Aug;32(16):3321-32. doi: 10.1128/MCB.00296-12. Epub 2012 Jun 18.
36. Expression and proteolytic activity of calpain in lens epithelial cells of oxidative cataract. Xu W, etal., J Zhejiang Univ Sci. 2004 Jun;5(6):743-8.
37. Calpain-2 contributes to neuropathic pain following motor nerve injury via up-regulating interleukin-6 in DRG neurons. Zang Y, etal., Brain Behav Immun. 2015 Feb;44:37-47. doi: 10.1016/j.bbi.2014.08.003. Epub 2014 Aug 20.
38. Cardiac protective effects of dexrazoxane on animal cardiotoxicity model induced by anthracycline combined with trastuzumab is associated with upregulation of calpain-2. Zhang S, etal., Medicine (Baltimore). 2015 Jan;94(4):e445. doi: 10.1097/MD.0000000000000445.
39. Calpain-mediated collapsin response mediator protein-1, -2, and -4 proteolysis after neurotoxic and traumatic brain injury. Zhang Z, etal., J Neurotrauma. 2007 Mar;24(3):460-72.
40. Subcellular localization and duration of mu-calpain and m-calpain activity after traumatic brain injury in the rat: a casein zymography study. Zhao X, etal., J Cereb Blood Flow Metab. 1998 Feb;18(2):161-7. doi: 10.1097/00004647-199802000-00006.
Additional References at PubMed
PMID:7635186   PMID:10949052   PMID:11102442   PMID:11342050   PMID:12150984   PMID:12534936   PMID:14559243   PMID:14618389   PMID:15132950   PMID:15489334   PMID:16433929   PMID:17712625  
PMID:18258589   PMID:18415939   PMID:19056867   PMID:19199708   PMID:19318376   PMID:19861418   PMID:20211186   PMID:20298691   PMID:20945043   PMID:21145877   PMID:21423176   PMID:21549862  
PMID:21849499   PMID:22547201   PMID:22555453   PMID:22870316   PMID:23376485   PMID:23495712   PMID:25270371   PMID:25820554   PMID:26086870   PMID:27622212   PMID:28342779   PMID:28559121  
PMID:29413901   PMID:29476059   PMID:29477696   PMID:29772491   PMID:30423475   PMID:33456665   PMID:33517223   PMID:33688783   PMID:34513987   PMID:36430329   PMID:36703913  


Genomics

Comparative Map Data
Capn2
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81396,681,902 - 96,732,625 (-)NCBIGRCr8
mRatBN7.21394,150,244 - 94,200,969 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1394,150,240 - 94,200,969 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1396,655,495 - 96,706,202 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01398,055,407 - 98,106,133 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01395,237,587 - 95,288,310 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.013100,878,649 - 100,928,811 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl13100,878,650 - 100,928,811 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.013105,814,749 - 105,864,911 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41398,473,367 - 98,524,463 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.11398,662,303 - 98,713,399 (-)NCBI
Celera1393,683,410 - 93,734,060 (-)NCBICelera
Cytogenetic Map13q26NCBI
CAPN2
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh381223,701,597 - 223,776,018 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl1223,701,593 - 223,776,018 (+)EnsemblGRCh38hg38GRCh38
GRCh371223,889,299 - 223,963,720 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 361221,966,742 - 222,030,343 (+)NCBINCBI36Build 36hg18NCBI36
Build 341220,206,935 - 220,270,453NCBI
Celera1197,044,917 - 197,119,643 (+)NCBICelera
Cytogenetic Map1q41NCBI
HuRef1194,501,759 - 194,576,134 (+)NCBIHuRef
CHM1_11225,161,051 - 225,236,057 (+)NCBICHM1_1
T2T-CHM13v2.01222,891,307 - 222,965,751 (+)NCBIT2T-CHM13v2.0
Capn2
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm391182,294,818 - 182,345,175 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl1182,294,825 - 182,345,173 (-)EnsemblGRCm39 Ensembl
GRCm381182,467,253 - 182,517,610 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl1182,467,260 - 182,517,608 (-)EnsemblGRCm38mm10GRCm38
MGSCv371184,397,390 - 184,447,614 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv361184,303,935 - 184,354,199 (-)NCBIMGSCv36mm8
Celera1189,509,702 - 189,560,154 (-)NCBICelera
Cytogenetic Map1H5NCBI
cM Map184.93NCBI
Capn2
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049555201,286,356 - 1,315,328 (-)EnsemblChiLan1.0
ChiLan1.0NW_0049555201,287,829 - 1,315,318 (-)NCBIChiLan1.0ChiLan1.0
CAPN2
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v2125,592,267 - 25,655,726 (-)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan1125,548,169 - 25,611,611 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v01199,335,582 - 199,399,267 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.11204,346,476 - 204,410,137 (+)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl1204,335,573 - 204,409,150 (+)Ensemblpanpan1.1panPan2
CAPN2
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1740,333,379 - 40,367,158 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl740,334,012 - 40,377,037 (-)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha739,815,620 - 39,853,714 (-)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0740,166,074 - 40,204,194 (-)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl740,166,086 - 40,204,215 (-)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1740,007,852 - 40,045,930 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0740,016,382 - 40,054,477 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0740,285,433 - 40,323,542 (-)NCBIUU_Cfam_GSD_1.0
Capn2
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_02440934453,814,785 - 53,867,532 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_004936526879,765 - 932,682 (+)EnsemblSpeTri2.0SpeTri2.0 Ensembl
SpeTri2.0NW_004936526879,765 - 932,682 (+)NCBISpeTri2.0SpeTri2.0SpeTri2.0
CAPN2
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl1019,758,757 - 19,820,246 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.11019,758,824 - 19,820,241 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
CAPN2
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1255,845,873 - 5,905,464 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl255,846,298 - 5,905,402 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_0236660556,059,645 - 6,119,546 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0

Variants

.
Variants in Capn2
696 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:366
Count of miRNA genes:212
Interacting mature miRNAs:237
Transcripts:ENSRNOT00000045326
Prediction methods:Microtar, Miranda, Rnahybrid
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (GRCr8)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
7207885Glom27Glomerulus QTL 273.9kidney glomerulus integrity trait (VT:0010546)kidney crescentic glomeruli count to kidney normal glomeruli count ratio (CMO:0002139)1320605871101339738Rat
7387280Uae43Urinary albumin excretion QTL 435.690.4174urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)1366451204106807694Rat
2293702Bss34Bone structure and strength QTL 344.610.0001femur strength trait (VT:0010010)femur midshaft polar moment of inertia (CMO:0001669)1365103704106807694Rat
1354621Rf47Renal function QTL 473.7kidney renin amount (VT:0010559)kidney renin level (CMO:0002166)1330395351101056920Rat
1354655Bp241Blood pressure QTL 2413.9arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)1356056920101056920Rat
4889606Gluco63Glucose level QTL 632.860.003blood glucose amount (VT:0000188)blood glucose level area under curve (AUC) (CMO:0000350)1380753256106807694Rat
8655959Pur32Proteinuria QTL 328.4urine total protein amount (VT:0000032)urine total protein excretion rate (CMO:0000756)137402391897213863Rat
1641901Alcrsp6Alcohol response QTL 6response to alcohol trait (VT:0010489)duration of loss of righting reflex (CMO:0002289)135236217197362171Rat
2293687Bss26Bone structure and strength QTL 264.60.0001femur morphology trait (VT:0000559)femur cross-sectional area (CMO:0001661)1365103704106807694Rat
12879475Bp400Blood pressure QTL 400arterial blood pressure trait (VT:2000000)mean arterial blood pressure (CMO:0000009)1361825626106807694Rat
1581570Eae17Experimental allergic encephalomyelitis QTL 174.1nervous system integrity trait (VT:0010566)experimental autoimmune encephalomyelitis incidence/prevalence measurement (CMO:0001046)138897350101631289Rat
1354666Bp244Blood pressure QTL 2444.9arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)131101056920Rat
2293341Glom15Glomerulus QTL 159.1kidney glomerulus integrity trait (VT:0010546)kidney sclerotic glomeruli count to total glomeruli count ratio (CMO:0001269)1374862117101339893Rat

Markers in Region
D13Wox20  
Rat AssemblyChrPosition (strand)SourceJBrowse
Cytogenetic Map13q26UniSTS
RH136960  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21394,150,268 - 94,150,456 (+)MAPPERmRatBN7.2
Rnor_6.013100,878,674 - 100,878,861NCBIRnor6.0
Rnor_5.013105,814,774 - 105,814,961UniSTSRnor5.0
RGSC_v3.41398,473,392 - 98,473,579UniSTSRGSC3.4
Celera1393,683,435 - 93,683,622UniSTS
Cytogenetic Map13q26UniSTS
RH138755  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21394,192,571 - 94,192,736 (+)MAPPERmRatBN7.2
Rnor_6.013100,920,414 - 100,920,578NCBIRnor6.0
Rnor_5.013105,856,514 - 105,856,678UniSTSRnor5.0
RGSC_v3.41398,516,066 - 98,516,230UniSTSRGSC3.4
Celera1393,725,663 - 93,725,827UniSTS
RH 3.4 Map13632.9UniSTS
Cytogenetic Map13q26UniSTS


Expression

RNA-SEQ Expression

alimentary part of gastrointestinal system
appendage
circulatory system
ectoderm
endocrine system
endoderm
exocrine system
hemolymphoid system
hepatobiliary system
integumental system
mesenchyme
mesoderm
nervous system
renal system
reproductive system
respiratory system
9 11 49 113 91 90 59 25 59 6 218 97 93 45 60 31

Sequence


Ensembl Acc Id: ENSRNOT00000045326   ⟹   ENSRNOP00000046509
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1394,150,245 - 94,200,969 (-)Ensembl
Rnor_6.0 Ensembl13100,878,650 - 100,928,811 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000097310   ⟹   ENSRNOP00000086926
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1394,150,240 - 94,200,561 (-)Ensembl
Ensembl Acc Id: ENSRNOT00000118482   ⟹   ENSRNOP00000076404
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1394,153,195 - 94,200,969 (-)Ensembl
RefSeq Acc Id: NM_017116   ⟹   NP_058812
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr81396,681,902 - 96,732,625 (-)NCBI
mRatBN7.21394,150,244 - 94,200,969 (-)NCBI
Rnor_6.013100,878,649 - 100,928,811 (-)NCBI
Rnor_5.013105,814,749 - 105,864,911 (-)NCBI
RGSC_v3.41398,473,367 - 98,524,463 (-)RGD
Celera1393,683,410 - 93,734,060 (-)RGD
Sequence:
RefSeq Acc Id: NP_058812   ⟸   NM_017116
- UniProtKB: Q07009 (UniProtKB/Swiss-Prot),   A6JGL9 (UniProtKB/TrEMBL)
- Sequence:
Ensembl Acc Id: ENSRNOP00000046509   ⟸   ENSRNOT00000045326
Ensembl Acc Id: ENSRNOP00000076404   ⟸   ENSRNOT00000118482
Ensembl Acc Id: ENSRNOP00000086926   ⟸   ENSRNOT00000097310
Protein Domains
Calpain catalytic   EF-hand

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-Q07009-F1-model_v2 AlphaFold Q07009 1-700 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13699078
Promoter ID:EPDNEW_R9603
Type:initiation region
Name:Capn2_1
Description:calpain 2
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.013100,928,488 - 100,928,548EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:2268 AgrOrtholog
BioCyc Gene G2FUF-17074 BioCyc
Ensembl Genes ENSRNOG00000034015 Ensembl, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000045326.4 UniProtKB/Swiss-Prot
  ENSRNOT00000097310.1 UniProtKB/TrEMBL
  ENSRNOT00000118482.1 UniProtKB/TrEMBL
Gene3D-CATH 2.60.120.380 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Cysteine proteinases UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF-hand UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:5621252 IMAGE-MGC_LOAD
InterPro C2_III UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Calpain_cysteine_protease UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Calpain_domain_III UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Calpain_III UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Calpain_III_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF-hand-dom_pair UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_Hand_1_Ca_BS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_hand_dom UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFh_PEF_CAPN2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Papain-like_cys_pep_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Pept_cys_AS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Peptidase_C2_calpain_cat UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:29154 UniProtKB/Swiss-Prot
MGC_CLONE MGC:72508 IMAGE-MGC_LOAD
NCBI Gene 29154 ENTREZGENE
PANTHER CALPAIN UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PTHR10183:SF268 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam Calpain_III UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF-hand_8 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Peptidase_C2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Capn2 PhenoGen
PRINTS CALPAIN UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PROSITE CALPAIN_CAT UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_HAND_1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EF_HAND_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  THIOL_PROTEASE_CYS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000034015 RatGTEx
  ENSRNOG00055012648 RatGTEx
  ENSRNOG00060007713 RatGTEx
  ENSRNOG00065017813 RatGTEx
SMART calpain_III UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  CysPc UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Superfamily-SCOP SSF47473 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF49758 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF54001 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A8I5Y510_RAT UniProtKB/TrEMBL
  A0A8I6A3B4_RAT UniProtKB/TrEMBL
  A6JGL9 ENTREZGENE, UniProtKB/TrEMBL
  CAN2_RAT UniProtKB/Swiss-Prot, ENTREZGENE


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2016-01-27 Capn2  calpain 2  Capn2  calpain 2, (m/II) large subunit  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2012-01-06 Capn2  calpain 2, (m/II) large subunit  Capn2  calpain 2  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2002-06-10 Capn2  calpain 2      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_protein 700 amino acid protein 69794
gene_transcript contains 21 exons 69794